ID   THIM_CLOP1              Reviewed;         265 AA.
AC   Q0TQV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Hydroxyethylthiazole kinase;
DE            EC=2.7.1.50;
DE   AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase;
DE            Short=Thz kinase;
DE            Short=TH kinase;
GN   Name=thiM; OrderedLocusNames=CPF_1544;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole =
CC       ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine pyrophosphate
CC       biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 4-methyl-
CC       5-(2-hydroxyethyl)-thiazole: step 1/1.
CC   -!- SIMILARITY: Belongs to the Thz kinase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000246; ABG83081.1; -; Genomic_DNA.
DR   RefSeq; YP_695987.1; -.
DR   GeneID; 4201531; -.
DR   GenomeReviews; CP000246_GR; CPF_1544.
DR   KEGG; cpf:CPF_1544; -.
DR   TIGR; CPF_1544; -.
DR   HOGENOM; Q0TQV3; -.
DR   OMA; Q0TQV3; ASPVMAH.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:HAMAP.
DR   GO; GO:0009228; P:thiamin biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00228; -; 1.
DR   InterPro; IPR000417; Hyethyz_kinase.
DR   InterPro; IPR011144; Hyethyz_kinsmonf.
DR   PANTHER; PTHR20857:SF14; Hyethyz_kinase; 1.
DR   Pfam; PF02110; HK; 1.
DR   PIRSF; PIRSF000513; Thz_kinase; 1.
DR   PRINTS; PR01099; HYETHTZKNASE.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    265       Hydroxyethylthiazole kinase.
FT                                /FTId=PRO_1000021505.
FT   BINDING      36     36       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     112    112       ATP (By similarity).
FT   BINDING     160    160       ATP (By similarity).
FT   BINDING     187    187       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   265 AA;  29495 MW;  0E3E82BF9B81CD59 CRC64;
     MEVLKRENPL IHMITNYVTV NDLAQVTINY GGLPLMATHH DELKEITKMA NGLLVNIGTL
     EPYQMESSMI SMKIAKEKGI PSVLDPVGVQ ASKLRKDFAK KLILEGEPSL IKGNLAEIKT
     LIGETSNSIG IDSFDDSLSE NTKNKIKEYA RERNLIVVVS GVVDFITNGE ESASVKNGTY
     KMSKITGTGC MLGALLTLAL SFYDHKDLRF KEVVKAVSTW GICGELAEER LREKEGLMTF
     KHNLLDELSI INDETIKERE KVIYD
//